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TPP2_MOUSE
ID   TPP2_MOUSE              Reviewed;        1262 AA.
AC   Q64514; Q5D072;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Tripeptidyl-peptidase 2;
DE            Short=TPP-2;
DE            EC=3.4.14.10 {ECO:0000250|UniProtKB:P29144};
DE   AltName: Full=Tripeptidyl aminopeptidase;
DE   AltName: Full=Tripeptidyl-peptidase II;
DE            Short=TPP-II;
GN   Name=Tpp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC   STRAIN=Leaden X A1;
RX   PubMed=7998988; DOI=10.1042/bj3040517;
RA   Tomkinson B.;
RT   "Characterization of cDNA for murine tripeptidyl-peptidase II reveals
RT   alternative splicing.";
RL   Biochem. J. 304:517-523(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   ASP-44.
RX   PubMed=17932511; DOI=10.1038/sj.embor.7401086;
RA   McKay R.M., McKay J.P., Suh J.M., Avery L., Graff J.M.;
RT   "Tripeptidyl peptidase II promotes fat formation in a conserved fashion.";
RL   EMBO Rep. 8:1183-1189(2007).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19747897; DOI=10.1016/j.bbrc.2009.09.021;
RA   Preta G., de Klark R., Glas R.;
RT   "A role for nuclear translocation of tripeptidyl-peptidase II in reactive
RT   oxygen species-dependent DNA damage responses.";
RL   Biochem. Biophys. Res. Commun. 389:575-579(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-401, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Cytosolic tripeptidyl-peptidase that releases N-terminal
CC       tripeptides from polypeptides and is a component of the proteolytic
CC       cascade acting downstream of the 26S proteasome in the ubiquitin-
CC       proteasome pathway. It plays an important role in intracellular amino
CC       acid homeostasis (By similarity). Stimulates adipogenesis
CC       (PubMed:17932511). {ECO:0000250|UniProtKB:P29144,
CC       ECO:0000269|PubMed:17932511}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC         EC=3.4.14.10; Evidence={ECO:0000250|UniProtKB:P29144};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19747897}. Nucleus
CC       {ECO:0000269|PubMed:19747897}. Note=Translocates to the nucleus in
CC       response to gamma-irradiation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q64514-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q64514-2; Sequence=VSP_005446;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, skeletal muscle, gonadal
CC       and mesenteric white adipose tissue and brown adipose tissues.
CC       {ECO:0000269|PubMed:17932511}.
CC   -!- DISRUPTION PHENOTYPE: Homozygous mutant mice die in utero before
CC       embryonic day 9.0. Heterozygous mice display normal food intake but
CC       appear lean with a significant reduction in body fat, smaller
CC       adipocytes, decreased plasma insulin levels and less white adipose
CC       tissue in the gonad, groin and mesenteric regions.
CC       {ECO:0000269|PubMed:17932511}.
CC   -!- MISCELLANEOUS: The limitation of proteolytic products to tripeptides is
CC       achieved by tailoring the size of the substrate-binding cleft: the two
CC       negatively charged residues Glu-305 and Glu-331 that are blocking
CC       position P4 limit the number of residues that can be accommodated in
CC       the binding cleft and thus create a molecular ruler. At the same time,
CC       they orient substrates so that the tripeptides are removed exclusively
CC       from the N-terminus (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; X81323; CAA57103.1; -; mRNA.
DR   EMBL; BC058239; AAH58239.1; -; mRNA.
DR   CCDS; CCDS14926.1; -. [Q64514-1]
DR   CCDS; CCDS78577.1; -. [Q64514-2]
DR   PIR; I48855; I48855.
DR   RefSeq; NP_001297469.1; NM_001310540.1. [Q64514-2]
DR   RefSeq; NP_033444.1; NM_009418.3. [Q64514-1]
DR   AlphaFoldDB; Q64514; -.
DR   SMR; Q64514; -.
DR   BioGRID; 204295; 5.
DR   CORUM; Q64514; -.
DR   IntAct; Q64514; 1.
DR   STRING; 10090.ENSMUSP00000085244; -.
DR   ChEMBL; CHEMBL5512; -.
DR   MEROPS; S08.A56; -.
DR   iPTMnet; Q64514; -.
DR   PhosphoSitePlus; Q64514; -.
DR   SwissPalm; Q64514; -.
DR   EPD; Q64514; -.
DR   jPOST; Q64514; -.
DR   MaxQB; Q64514; -.
DR   PaxDb; Q64514; -.
DR   PeptideAtlas; Q64514; -.
DR   PRIDE; Q64514; -.
DR   ProteomicsDB; 258830; -. [Q64514-1]
DR   ProteomicsDB; 258831; -. [Q64514-2]
DR   Antibodypedia; 11138; 138 antibodies from 26 providers.
DR   DNASU; 22019; -.
DR   Ensembl; ENSMUST00000087933; ENSMUSP00000085244; ENSMUSG00000041763. [Q64514-1]
DR   Ensembl; ENSMUST00000188313; ENSMUSP00000139918; ENSMUSG00000041763. [Q64514-2]
DR   GeneID; 22019; -.
DR   KEGG; mmu:22019; -.
DR   UCSC; uc007avs.1; mouse. [Q64514-1]
DR   UCSC; uc007avt.1; mouse. [Q64514-2]
DR   CTD; 7174; -.
DR   MGI; MGI:102724; Tpp2.
DR   VEuPathDB; HostDB:ENSMUSG00000041763; -.
DR   eggNOG; KOG1114; Eukaryota.
DR   GeneTree; ENSGT00390000014623; -.
DR   InParanoid; Q64514; -.
DR   OMA; SLRDFQC; -.
DR   OrthoDB; 156304at2759; -.
DR   PhylomeDB; Q64514; -.
DR   TreeFam; TF105647; -.
DR   BRENDA; 3.4.14.10; 3474.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   BioGRID-ORCS; 22019; 1 hit in 58 CRISPR screens.
DR   ChiTaRS; Tpp2; mouse.
DR   PRO; PR:Q64514; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q64514; protein.
DR   Bgee; ENSMUSG00000041763; Expressed in spermatid and 245 other tissues.
DR   ExpressionAtlas; Q64514; baseline and differential.
DR   Genevisible; Q64514; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0042277; F:peptide binding; ISO:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008240; F:tripeptidyl-peptidase activity; ISO:MGI.
DR   GO; GO:0080144; P:amino acid homeostasis; ISO:MGI.
DR   GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04857; Peptidases_S8_Tripeptidyl_Aminopeptidase_II; 1.
DR   Gene3D; 3.40.50.200; -; 2.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR022229; Peptidase_S8A_TPPII.
DR   InterPro; IPR034051; TPP_II_domain.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF12580; TPPII; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Aminopeptidase; Cytoplasm; Hydrolase;
KW   Nucleus; Phosphoprotein; Protease; Reference proteome; Serine protease.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P29144"
FT   CHAIN           2..1262
FT                   /note="Tripeptidyl-peptidase 2"
FT                   /id="PRO_0000076423"
FT   DOMAIN          9..508
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   REGION          1010..1030
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1030
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        44
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        264
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        449
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P29144"
FT   MOD_RES         401
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         915
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29144"
FT   VAR_SEQ         985..997
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:7998988"
FT                   /id="VSP_005446"
FT   MUTAGEN         44
FT                   /note="D->A: No effect on adipogenesis."
FT                   /evidence="ECO:0000269|PubMed:17932511"
SQ   SEQUENCE   1262 AA;  139879 MW;  D50D22C85544B034 CRC64;
     MATAATEEPF PFHGLLPKKE TGASSFLCRY PEYDGRGVLI AVLDTGVDPG APGMQVTTDG
     KPKIIDIIDT TGSGDVNTAT EVEPKDGEII GLSGRVLKIP ANWTNPLGKY HIGIKNGYDF
     YPKALKERIQ KERKEKIWDP IHRVALAEAC RKQEEFDIAN NGSSQANKLI KEELQSQVEL
     LNSFEKKYSD PGPVYDCLVW HDGETWRACV DSNENGDLSK CAVLRNYKEA QEYSSFGTAE
     MLNYSVNIYD DGNLLSIVTS GGAHGTHVAS IAAGHFPEEP ERNGVAPGAQ ILSIKIGDTR
     LSTMETGTGL IRAMIEVINH KCDLVNYSYG EATHWPNSGR ICEVINEAVW KHNTIYVSSA
     GNNGPCLSTV GCPGGTTSSV IGVGAYVSPD MMVAEYSLRE KLPANQYTWS SRGPSADGAL
     GVSISAPGGA IASVPNWTLR GTQLMNGTSM SSPNACGGIA LVLSGLKANN VDYTVHSVRR
     ALENTAIKAD NIEVFAQGHG IIQVDKAYDY LIQNTSFANR LGFTVTVGNN RGIYLRDPVQ
     VAAPSDHGVG IEPVFPENTE NSEKISFQLH LALTSNSSWV QCPSHLELMN QCRHINIRVD
     PRGLREGLHY TEVCGYDIAS PNAGPLFRVP ITAVIAAKVN ESSHYDLAFT DVHFKPGQIR
     RHFVEVPEGA TWAEVTVCSC SSEVSAKFVL HAVQLVKQRA YRSHEFYKFC SLPEKGTLIE
     AFPVLGGKAI EFCIARWWAS LSDVNIDYTI SFHGIVCTAP QLNIHASEGI NRFDVQSSLK
     YEDLAPCITL KSWVQTLRPV NAKTRPLGSR DVLPNNRQLY EMVLTYSFHQ PKSGEVTPSC
     PLLCELLYES EFDSQLWIIF DQNKRQMGSG DAYPHQYSLK LEKGDYTIRL QIRHEQISDL
     DRLKDLPFIV SHRLSNTLSL DIHENHSLAL LGKKKSSSLT LPPKYNQPFF VTSLPDDKIP
     KGAGPGCYLA GSLTLSKTEL GKKAGQSAAK RQGKFKKDVI PVHYYLIPPP TKIKNGSKDK
     EKDSEKEKDL KEEFTEALRD LKIQWMTKLD STDIYNELKE TYPAYLPLYV ARLHQLDAEK
     ERMKRLNEIV DAANAVISHI DQTALAVYIA MKTDPRPDAA TIKNDMDKQK STLIDALCRK
     GCALADHLLH TQPHDGAAAG DAEAKEEEGE STMESLSETY WETTKWTDLF DTKVLIFAYK
     HALVNKMYGR GLKFATKLVE EKPTKENWKN CIQLMKLLGW THCASFTENW LPIMYPPDYC
     VF
 
 
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